The molecular basis of alcohol actions in the nervous system is poorly understood. This project combined molecular biological and electrophysiological techniques to study the molecular mechanisms of alcohol action using Xenopus oocytes as an expression system. A study of straight chain aliphatic alcohols on the response of recombinant GluR3 receptors showed that potency for inhibition of the response decreased with heptanol and octanol, and nonanol did not inhibit the response. This indicates that these alcohols exhibit a potency cutoff for inhibition of non-NMDA glutamate receptors. A study of the ethanol sensitivity of recombinant n4/~1 NMDA receptor subunits showed that these subunits exhibit an ethanol sensitivity similar to that of the n3/~1 subunits. A study of ethanol and glycine on recombinant n1/~1, n2/~1, n3/~1, and n4/~1 NMDA receptor subunits revealed that ethanol is not competitive with glycine for any of these subunit combinations. A study of the effect of ethanol on recombinant nACh`7 receptors showed that ethanol produced a non-competitive inhibition of this receptor. A study on the effect of ethanol on recombinant 5-HT3 receptors showed that ethanol potentiated the current activated by low concentrations of 5-HT, but did not augment the current activated by high agonist concentrations. A study of a chimeric receptor, with the N-terminal domain from the nACh`7 receptor and the transmembrane and C-terminal domains from the 5- HT3 receptor, found that the response of the chimeric receptor was inhibited by ethanol. This inhibition was not significantly different from the ethanol inhibition of nACh`7 receptors, suggesting that the ethanol inhibition of this receptor is mediated by the N-terminal domain of the receptor. The observations suggest that combining molecular biological and electrophysiological techniques will be a useful approach for elucidating the molecular determinants of alcohol actions in the nervous system.